TRPB2_PYRFU
ID TRPB2_PYRFU Reviewed; 446 AA.
AC Q8U0J5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Tryptophan synthase beta chain 2;
DE EC=4.2.1.20;
GN Name=trpB2; OrderedLocusNames=PF1592;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81716.1; -; Genomic_DNA.
DR RefSeq; WP_011012738.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0J5; -.
DR SMR; Q8U0J5; -.
DR STRING; 186497.PF1592; -.
DR PRIDE; Q8U0J5; -.
DR EnsemblBacteria; AAL81716; AAL81716; PF1592.
DR GeneID; 41713416; -.
DR KEGG; pfu:PF1592; -.
DR PATRIC; fig|186497.12.peg.1658; -.
DR eggNOG; arCOG01432; Archaea.
DR HOGENOM; CLU_042858_1_0_2; -.
DR OMA; MLHQTII; -.
DR OrthoDB; 24741at2157; -.
DR PhylomeDB; Q8U0J5; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR006316; Trp_synth_b-like.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR48077:SF6; PTHR48077:SF6; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR PIRSF; PIRSF500824; TrpB_prok; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01415; trpB_rel; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..446
FT /note="Tryptophan synthase beta chain 2"
FT /id="PRO_0000099051"
FT MOD_RES 110
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 446 AA; 49616 MW; 11564BFD6C41A64F CRC64;
MKVVLPDGRI PRRWYNILPD LPEPLAPPLD PETNEPVDPK KLERIFAKEL VKQEMSTKRY
IKIPEEVRKM YSKIGRPTPL FRATNLEKYL NTPARIYFKF EGATVTGSHK INTALAQAYY
AKKEGIERLV TETGAGQWGT ALSLAGALMG IKVRVYMARA SYEQKPYRKV LMRIYGAEVF
PSPSENTEIG KRFLSENPNH PGSLGIAISE AIEDVLKDEK ARYSLGSVLN HVLMHQTVIG
LEAKQQMEEF EEPDVIIGCV GGGSNFAGLA YPFVKEVLDG DNEYEFIAVE PKAAPSMTRG
VYTYDFGDSG ELTPKLKMHT LGHRYHVPPI HAGGLRYHGV APTLSVLVNN GIVKPIAYHQ
TEVFEAAALF AKLEGIVPAP ESAHAIKATI DKAIEAKREG KEIVILFNLS GHGLLDLHGY
EEYLEGRLQD YEPKDLPISN PLNPKP